Journal:FEBS Open Bio:1: Difference between revisions
From Proteopedia
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
Biotin-dependent acetyl-CoA carboxylases catalyze the committed step in type II fatty acid biosynthesis, the main route for production of membrane phospholipids in bacteria, and are considered a key target for antibacterial drug discovery. Here we describe the first structure of AccA3, an essential component of the acetyl-CoA carboxylase system in ''Mycobacterium tuberculosis'' (MTb). The structure, sequence comparisons, and modeling of ligand-bound states reveal that the ATP cosubstrate-binding site shows distinct differences compared to other bacterial and eukaryotic biotin carboxylases, including all human homologs. This suggests the possibility to design MTb AccA3 subtype-specific inhibitors. | Biotin-dependent acetyl-CoA carboxylases catalyze the committed step in type II fatty acid biosynthesis, the main route for production of membrane phospholipids in bacteria, and are considered a key target for antibacterial drug discovery. Here we describe the first structure of AccA3, an essential component of the acetyl-CoA carboxylase system in ''Mycobacterium tuberculosis'' (MTb). The structure, sequence comparisons, and modeling of ligand-bound states reveal that the ATP cosubstrate-binding site shows distinct differences compared to other bacterial and eukaryotic biotin carboxylases, including all human homologs. This suggests the possibility to design MTb AccA3 subtype-specific inhibitors. | ||
''Mycobacterium tuberculosis'' <scene name='76/763765/Cv/2'>AccA3 adopts the ATPgrasp superfamily fold</scene>, and crystallized as a | |||
<scene name='76/763765/Cv/3'>dimer in the asymmetric unit</scene>. <scene name='76/763765/Cv/4'>The lack of an ordered structure for domain B in chain B</scene>. | |||
</StructureSection> | </StructureSection> | ||
<references/> | <references/> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For additional details please see I3DC.
